Conformational variability of chicken cystatin. Comparison of structures determined by X-ray diffraction and NMR spectroscopy.

@article{Engh1993ConformationalVO,
  title={Conformational variability of chicken cystatin. Comparison of structures determined by X-ray diffraction and NMR spectroscopy.},
  author={Richard Alan Engh and Thorsten Dieckmann and Wolfram Bode and Ennes A. Auerswald and Vito Turk and Robert Huber and Hartmut Oschkinat},
  journal={Journal of molecular biology},
  year={1993},
  volume={234 4},
  pages={1060-9}
}
The structural model derived from X-ray crystallography for unphosphorylated wild-type chicken cystatin is compared with two chicken cystatin structures derived from NMR spectroscopy: the phosphorylated wild-type and the genetically engineered variant AEF-SIM-M29I-M89L. The comparison shows the same overall fold, but also significant differences in structurally variable segments of the polypeptide chain. The largest such segment, comprising residues 71 to 89, is a region characteristic of the… CONTINUE READING